These cells were scratch-wounded followed by fixation 12-hours post-wounding. Tubulin (Green) and alpha-mannosidase II (Red) were labeled to note cell polarization and Golgi orientation. Cells expressing paxillin lacking LD4 are unable to reorient the Golgi towards the wound edge. From the lab of Christopher Turner, PhD.
Biochemistry and cell biology of formins as actin cytoskeleton organizers, using Caenorhabditis elegans as a model system.
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The actin cytoskeleton is a network of filaments composed of the protein actin that populate the cell's cytoplasm. In a given cell, this network can be organized into a large number of distinct substructures that may range form from simple cable-like bundles through complex, repetitive arrays. These cytoskeletal structures give cells their proper shape, control the distribution of organelles, and allow cells to move. Our primary goal is to understand at the molecular level how distinct actin filament structures assemble, and how they perform their functions. Our focus is on the family of actin-organizing proteins called Formins. Formins are conserved proteins with homologs in nearly every type of eukaryotic organism, including animals, plants, and fungi. Among animals, seven distinct subclasses of Formins exist, but their precise functions are not clear. We are probing the functions of these Formin subclasses through a combination of biochemical assays using purified proteins, and genetic and microscopic studies using the model organism Caenorhabditis elegans. Our current work focuses on the relationship between one Formin subclass and muscle development.